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Q03529

- SCS7_YEAST

UniProt

Q03529 - SCS7_YEAST

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Protein

Ceramide very long chain fatty acid hydroxylase SCS7

Gene

SCS7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3.6 Publications

Cofactori

Iron.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi72 – 721Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. fatty acid alpha-hydroxylase activity Source: SGD
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. inositolphosphoceramide metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13537.
YEAST:YMR272C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide very long chain fatty acid hydroxylase SCS7 (EC:1.-.-.-)
Short name:
Ceramide VLCFA hydroxylase SCS7
Alternative name(s):
Suppressor of calcium sensitivity 7
Gene namesi
Name:SCS7
Synonyms:FAH1
Ordered Locus Names:YMR272C
ORF Names:YM8156.14C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR272c.
SGDiS000004885. SCS7.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Ceramide very long chain fatty acid hydroxylase SCS7PRO_0000185407Add
BLAST

Proteomic databases

MaxQBiQ03529.
PaxDbiQ03529.
PeptideAtlasiQ03529.

Expressioni

Gene expression databases

GenevestigatoriQ03529.

Interactioni

Protein-protein interaction databases

BioGridi35451. 526 interactions.
IntActiQ03529. 34 interactions.
MINTiMINT-4498866.
STRINGi4932.YMR272C.

Structurei

3D structure databases

ProteinModelPortaliQ03529.
SMRiQ03529. Positions 13-85.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 196196CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini218 – 2225LumenalSequence Analysis
Topological domaini244 – 29754CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini319 – 35234LumenalSequence AnalysisAdd
BLAST
Topological domaini374 – 38411CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei197 – 21721HelicalSequence AnalysisAdd
BLAST
Transmembranei223 – 24321HelicalSequence AnalysisAdd
BLAST
Transmembranei298 – 31821HelicalSequence AnalysisAdd
BLAST
Transmembranei353 – 37321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 9082Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3000.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
InParanoidiQ03529.
OMAiMKAHHVK.
OrthoDBiEOG7RNK98.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Ino-phos-ceramide-B_Hydrxlase.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03529-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE
60 70 80 90 100
SILDYAGKDI TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT
110 120 130 140 150
NKNHKVEVQL SADGTEFDST TFVKELPAEE KLSIATDYSN DYKKHKFLDL
160 170 180 190 200
NRPLLMQILR SDFKKDFYVD QIHRPRHYGK GSAPLFGNFL EPLTKTAWWV
210 220 230 240 250
VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE YGLHRFLFHF
260 270 280 290 300
DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF
310 320 330 340 350
ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY
360 370 380
KNYQLGFGVT SWFWDEVFGT YLGPDAPLSK MKYE
Length:384
Mass (Da):44,881
Last modified:November 1, 1997 - v1
Checksum:iDF4BA5F2E0EA2218
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49260 Genomic DNA. Translation: CAA89255.1.
AY693150 Genomic DNA. Translation: AAT93169.1.
BK006946 Genomic DNA. Translation: DAA10172.1.
PIRiS54484.
RefSeqiNP_013999.1. NM_001182779.1.

Genome annotation databases

EnsemblFungiiYMR272C; YMR272C; YMR272C.
GeneIDi855315.
KEGGisce:YMR272C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49260 Genomic DNA. Translation: CAA89255.1 .
AY693150 Genomic DNA. Translation: AAT93169.1 .
BK006946 Genomic DNA. Translation: DAA10172.1 .
PIRi S54484.
RefSeqi NP_013999.1. NM_001182779.1.

3D structure databases

ProteinModelPortali Q03529.
SMRi Q03529. Positions 13-85.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35451. 526 interactions.
IntActi Q03529. 34 interactions.
MINTi MINT-4498866.
STRINGi 4932.YMR272C.

Proteomic databases

MaxQBi Q03529.
PaxDbi Q03529.
PeptideAtlasi Q03529.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR272C ; YMR272C ; YMR272C .
GeneIDi 855315.
KEGGi sce:YMR272C.

Organism-specific databases

CYGDi YMR272c.
SGDi S000004885. SCS7.

Phylogenomic databases

eggNOGi COG3000.
GeneTreei ENSGT00390000002142.
HOGENOMi HOG000023981.
InParanoidi Q03529.
OMAi MKAHHVK.
OrthoDBi EOG7RNK98.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13537.
YEAST:YMR272C-MONOMER.

Miscellaneous databases

NextBioi 979008.
PROi Q03529.

Gene expression databases

Genevestigatori Q03529.

Family and domain databases

Gene3Di 3.10.120.10. 1 hit.
InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Ino-phos-ceramide-B_Hydrxlase.
[Graphical view ]
Pfami PF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF005149. IPC-B_HD. 1 hit.
PRINTSi PR00363. CYTOCHROMEB5.
SUPFAMi SSF55856. SSF55856. 1 hit.
PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids."
    Mitchell A.G., Martin C.E.
    J. Biol. Chem. 272:28281-28288(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p."
    Haak D., Gable K., Beeler T., Dunn T.
    J. Biol. Chem. 272:29704-29710(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain."
    Dunn T.M., Haak D., Monaghan E., Beeler T.J.
    Yeast 14:311-321(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces cerevisiae."
    Swain E., Baudry K., Stukey J., McDonough V., Germann M., Nickels J.T. Jr.
    J. Biol. Chem. 277:26177-26184(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  11. "Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae."
    Guan X.L., Wenk M.R.
    Yeast 23:465-477(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro."
    Bosson R., Guillas I., Vionnet C., Roubaty C., Conzelmann A.
    Eukaryot. Cell 8:306-314(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSCS7_YEAST
AccessioniPrimary (citable) accession number: Q03529
Secondary accession number(s): D6W098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3290 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3